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| | <StructureSection load='1eha' size='340' side='right'caption='[[1eha]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='1eha' size='340' side='right'caption='[[1eha]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1eha]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EHA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EHA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1eha]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EHA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EHA FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1eh9|1eh9]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eha OCA], [https://pdbe.org/1eha PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eha RCSB], [https://www.ebi.ac.uk/pdbsum/1eha PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eha ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eha OCA], [https://pdbe.org/1eha PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eha RCSB], [https://www.ebi.ac.uk/pdbsum/1eha PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eha ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TREZ_SACSO TREZ_SACSO] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alpha-amylase]] | |
| - | [[Category: Atcc 35091]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Feese, M D]] | + | [[Category: Saccharolobus solfataricus]] |
| - | [[Category: Kato, M]] | + | [[Category: Feese MD]] |
| - | [[Category: Kato, Y]] | + | [[Category: Kato M]] |
| - | [[Category: Kobayashi, K]] | + | [[Category: Kato Y]] |
| - | [[Category: Komeda, T]] | + | [[Category: Kobayashi K]] |
| - | [[Category: Kuroki, R]] | + | [[Category: Komeda T]] |
| - | [[Category: Tamada, T]] | + | [[Category: Kuroki R]] |
| - | [[Category: Alpha-beta barrel]]
| + | [[Category: Tamada T]] |
| - | [[Category: Calcium binding]]
| + | |
| - | [[Category: Covalent dimer]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Sulfolobus solfataricus]]
| + | |
| - | [[Category: Trehalohydrolase]]
| + | |
| - | [[Category: Trehalose]]
| + | |
| Structural highlights
Function
TREZ_SACSO
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of glycosyltrehalose trehalohydrolase from the hyperthermophilic archaeum Sulfolobus solfataricus KM1 has been solved by multiple isomorphous replacement. The enzyme is an alpha-amylase (family 13) with unique exo-amylolytic activity for glycosyltrehalosides. It cleaves the alpha-1,4 glycosidic bond adjacent to the trehalose moiety to release trehalose and maltooligo saccharide. Unlike most other family 13 glycosidases, the enzyme does not require Ca(2+) for activity, and it contains an N-terminal extension of approximately 100 amino acid residues that is homologous to N-terminal domains found in many glycosidases that recognize branched oligosaccharides. Crystallography revealed the enzyme to exist as a homodimer covalently linked by an intermolecular disulfide bond at residue C298. The existence of the intermolecular disulfide bond was confirmed by biochemical analysis and mutagenesis. The N-terminal extension forms an independent domain connected to the catalytic domain by an extended linker. The functionally essential Ca(2+) binding site found in the B domain of alpha-amylases and many other family 13 glycosidases was found to be replaced by hydrophobic packing interactions. The enzyme also contains a very unusual excursion in the (beta/alpha)(8) barrel structure of the catalytic domain. This excursion originates from the bottom of the (beta/alpha)(8) barrel between helix 6 and strand 7, but folds upward in a distorted alpha-hairpin structure to form a part of the substrate binding cleft wall that is possibly critical for the enzyme's unique substrate selectivity. Participation of an alpha-beta loop in the formation of the substrate binding cleft is a novel feature that is not observed in other known (beta/alpha)(8) enzymes.
Crystal structure of glycosyltrehalose trehalohydrolase from the hyperthermophilic archaeum Sulfolobus solfataricus.,Feese MD, Kato Y, Tamada T, Kato M, Komeda T, Miura Y, Hirose M, Hondo K, Kobayashi K, Kuroki R J Mol Biol. 2000 Aug 11;301(2):451-64. PMID:10926520[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Feese MD, Kato Y, Tamada T, Kato M, Komeda T, Miura Y, Hirose M, Hondo K, Kobayashi K, Kuroki R. Crystal structure of glycosyltrehalose trehalohydrolase from the hyperthermophilic archaeum Sulfolobus solfataricus. J Mol Biol. 2000 Aug 11;301(2):451-64. PMID:10926520 doi:10.1006/jmbi.2000.3977
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